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Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...

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Revealing the Cytoskeletal Organization of Invasive Cancer Cells in 3D
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A Multicolor 3D-STORM High-Resolution Visualization Protocol for Collagen Mineralization in Self-Assembled

Wei Yin1, Guifeng Xiao1, Qianbing Zhao1

  • 1Core Facilities, Zhejiang University School of Medicine.

Journal of Visualized Experiments : Jove
|July 13, 2026
PubMed
Summary

This study introduces a multicolor 3D-STORM method for visualizing collagen mineralization at the nanoscale. The technique allows detailed 3D imaging of collagen, associated proteins, and mineral phases, advancing biomineralization research.

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Area of Science:

  • Biomaterials Science
  • Biomineralization
  • Tissue Engineering

Background:

  • Collagen mineralization is crucial for bone formation and integrity.
  • Understanding nanoscale mineralization dynamics requires advanced imaging techniques.
  • Current methods lack the resolution and specificity to visualize mineralization processes in detail.

Purpose of the Study:

  • To develop and present a multicolor 3D-STORM protocol for nanoscale visualization of collagen mineralization.
  • To enable simultaneous imaging of collagen, non-collagenous proteins, and mineral phases.
  • To provide a tool for detailed 3D analysis of intrafibrillar and extrafibrillar mineralization.

Main Methods:

  • Utilized a recombinant type I collagen self-assembled fibril model.
  • Employed multicolor 3D-STORM with multiplexed immunofluorescence labeling.
  • Sample preparation involved self-assembly, mineralization (ACP to HAP), and imaging in an oxygen-scavenging buffer.

Main Results:

  • Achieved nanoscale resolution (20-30 nm lateral, 50-60 nm axial) for 3D visualization.
  • Successfully imaged collagen networks, non-collagenous proteins (e.g., chondroitin sulfate), and calcium phosphate mineral phases.
  • Demonstrated clear intrafibrillar and extrafibrillar mineralization patterns with high correlation coefficients (Pearson's 0.89, Manders' 0.91).

Conclusions:

  • The developed 3D-STORM protocol offers unprecedented nanoscale insight into collagen mineralization.
  • This method provides a powerful tool for studying biomineralization dynamics in biomaterials and engineered tissues.
  • Facilitates a deeper understanding of mineralization processes relevant to bone tissue engineering and related fields.